Post-translational modifications of serotonin transporter

Anthonya Cooper; Donna Woulfe; Fusun Kilic

doi:10.1016/j.phrs.2018.10.018

Post-translational modifications of serotonin transporter

Pharmacol Res. 2019 Feb:140:7-13. doi: 10.1016/j.phrs.2018.10.018. Epub 2018 Oct 28.

Authors

Anthonya Cooper¹, Donna Woulfe², Fusun Kilic³

Affiliations

¹ Departments of Biochemistry and Molecular Biology, College of Medicine, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
² Department of Biological Sciences, University of Delaware, Newark, Delaware, USA.
³ Departments of Biochemistry and Molecular Biology, College of Medicine, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA. Electronic address: kilicfusun@uams.edu.

PMID: 30394319
DOI: 10.1016/j.phrs.2018.10.018

Abstract

The serotonin transporter (SERT) is an oligomeric glycoprotein with two sialic acid residues on each of two complex oligosaccharide molecules. Studies using in vivo and in vitro model systems demonstrated that diverse post-translational modifications, including phosphorylation, glycosylation, serotonylation, and disulfide bond formation, all favorably influences SERT conformation and allows the transporter to function most efficiently. This review discusses the post-translational modifications and their importance on the structure, maturation, and serotonin (5-HT) uptake ability of SERT. Finally, we discuss how these modifications are altered in diabetes mellitus and subsequently impairs the 5-HT uptake ability of SERT.

Keywords: Disulfide bond formation; Glycosylation; Insulin signaling; Oligomerization; SERT.

Publication types

Research Support, N.I.H., Extramural
Review

MeSH terms

Animals
Diabetes Mellitus / metabolism
Glycosylation
Humans
Phosphorylation
Protein Processing, Post-Translational*
Serotonin Plasma Membrane Transport Proteins / metabolism*

Substances

Serotonin Plasma Membrane Transport Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding